ID A0A2Y9T4E1_PHYMC Unreviewed; 700 AA.
AC A0A2Y9T4E1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Lipase maturation factor {ECO:0000256|RuleBase:RU361229};
GN Name=LMF2 {ECO:0000313|RefSeq:XP_023982954.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023982954.1};
RN [1] {ECO:0000313|RefSeq:XP_023982954.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_023982954.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Involved in the maturation of specific proteins in the
CC endoplasmic reticulum. {ECO:0000256|RuleBase:RU361229}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU361229}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU361229}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the lipase maturation factor family.
CC {ECO:0000256|ARBA:ARBA00005512, ECO:0000256|RuleBase:RU361229}.
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DR RefSeq; XP_023982954.1; XM_024127186.3.
DR AlphaFoldDB; A0A2Y9T4E1; -.
DR STRING; 9755.ENSPCTP00005025325; -.
DR KEGG; pcad:102996990; -.
DR InParanoid; A0A2Y9T4E1; -.
DR OrthoDB; 180704at2759; -.
DR Proteomes; UP000248484; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051604; P:protein maturation; IEA:InterPro.
DR InterPro; IPR009613; LMF.
DR PANTHER; PTHR14463; LIPASE MATURATION FACTOR; 1.
DR PANTHER; PTHR14463:SF5; LIPASE MATURATION FACTOR 2; 1.
DR Pfam; PF06762; LMF1; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU361229};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361229};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361229};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361229}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 128..145
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 310..334
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 368..386
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 398..422
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT REGION 657..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 700 AA; 79316 MW; B97243CD1CEFF49A CRC64;
MAGSRLPRQL FLQGVAAVFM FAFASLYMQI PGLYGPEGIL PARRTLRPQG KGRWRQLWET
PTLLWETPLL GLDTAQGLEL LSLLGTLLAL GALLLHQLRH LLVYLLLWAA YLSAYQVGQV
FLYFQWDSLL LETGFLALLV APLRLPPRHK QAQGRLAGVL PHEDLPFWLV RWLLFRLMFA
SGVVKLTSRC PAWWGLTALT YHFETQCLPT PASWFAHHLP VWLHKLGVVA TFLIEIAVPP
LFFAPVRRLR LAAFYSQVLL QVLIIITGNY NFFNLLTLLL TTALLDDAHL AARSGDSRRK
KTPTSWPKAL LALLALLLEL AVYGLLACGV VHYFGLEADW ERRAVRSKAT FTFHQFSQWL
KMVTLPTMWL GAASLAWELL TALWRWTHVR GWLRKCCAAV QLSVFGTATV ALFVISLVPY
SYMEPSTHGR LWTGAHRLFG TVEHLQLAHS YGLFRRMTGL GGRPEVVLEG SYDGHHWTEI
EFMYKPGNVS RAPPIVAPHQ PRLDWQMWFA ALGPHTHSPW FTSLVLRLLQ GKEPVIRLIQ
SHLPKYPFHK QPPTYVRAQR YKYRFSKPGE QGQWWQRQWV EEFFPSVSLG DPTLDMLLRQ
FGLQDKSPPR ARSSSNTLAQ ALRWMRKQLS PLEAPALLWG LLGTVGAIRV MQALLGPQSS
PRAKEEKHRP APAEDSVAAS KQASPAPDVS SGSQTPRRKK
//
